TY - JOUR AU - Mukherjee, Riddha AU - Paul, Tanmay AU - Halder, Suman Kumar AU - Soren, Jyoti Prakash AU - Banerjee, Amrita AU - Mondal, Keshab Chandra AU - Pati, Bikash Ranjan AU - Mohapatra, Pradeep Kumar Das PY - 2018/08/23 Y2 - 2024/03/29 TI - Characterization of an acidophilic α-amylase from Aspergillus niger RBP7 and study of catalytic potential in response to nutritionally important heterogeneous compound JF - Acta Biologica Szegediensis JA - Acta Biol Szeged VL - 62 IS - 1 SE - Articles DO - 10.14232/abs.2018.1.75-82 UR - https://abs.bibl.u-szeged.hu/index.php/abs/article/view/2946 SP - 75-82 AB - <p>An acidophilic α-amylase from <em>Aspergillus niger</em> RBP7 was purified after solid state fermentation on potato peel substrate. Molecular mass of the purified α-amylase was 37.5 kDa and it exhibited 1.4 mg/ml and 0.992 μ/mol/min K<sub>m</sub> and V<sub>max</sub> values, respectively. The enzyme was stable in the pH range from 2.0 to 6.0, at high NaCl concentration (3 M) and at temperatures between 40 °C and 70 °C. The enzyme showed an optimal activity at pH 3.0 and at 45 °C. The enzyme was inhibited by Hg<sup>2+</sup> and was stable in the presence of different surfactants (Tween 60, Tween 80, and SDS&nbsp;at 1% level) and different inhibitory reagents (β-mercaptoethanol, phenylmethylsulfonyl&nbsp;fluoride, and sodium azide). This acidophilic amylase enzyme can digest heterogeneous food materials, <em>i.e.</em> the mixture of rice, fish, bread and curry with comparable activity to&nbsp;the commercial diastase enzymes available.</p> ER -